ArticleThe protein journal2017
Heterologous Expression, Purification and Characterization of a Peroxidase Isolated from Lepidium draba.
Article in The protein journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 17 citations in OpenAlex.
- Covalent immobilization of Lepidium draba peroxidase on chitosan-coated magnetic nanoparticles and its application in glucose biosensing.Scientific reports · 2026Article
- Exploring the impact of taurine on the biochemical properties of urate oxidase: response surface methodology and molecular dynamics simulation.Journal of biological engineering · 2024Article
- Modeling and optimization of radish root extract drying as peroxidase source using spouted bed dryer.Scientific reports · 2021Article
- Scalable High-Performance Production of Recombinant Horseradish Peroxidase fromInternational journal of molecular sciences · 2020Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Peroxidase is one of the most widely used enzymes in biotechnology and medicine. In the current study, cDNA encoding peroxidase from Lepidium draba (LDP) was cloned and expressed in Escherichia coli BL21 (DE3) cells in the form of inclusion bodies (IBs). To achieve purified active enzyme, IBs were solubilized before being purified and refolded. The deduced amino acid sequence (308) of the LDP gene (924 bp) revealed 88.96% identity to horseradish peroxidase C1A (HRP C1A). The results of basic local alignment search tool (BLAST) and phylogenetic analysis of the protein sequence showed that this enzyme belongs to the neutral group of class III plant peroxidases. According to sequence analysis and structural modeling, critical amino acids in heme and calcium binding domain as well as cysteine residues were conserved as HRP C1A except for calcium binding domain where valine228 was replaced with isoleucine. The far-UV circular dichroism (CD) results were confirmed by homology modeling data showing the enzyme consists mainly of α-helices as other plant peroxidases. Overall, according to the results of catalytic activity and refolding yield, LDP can be introduced as a novel peroxidase for medical and biotechnology applications.
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Registered trials
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